CDN11_RANGI
ID CDN11_RANGI Reviewed; 12 AA.
AC P62566; P56245; P81253;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 10-FEB-2021, entry version 29.
DE RecName: Full=Caeridin-1.1/1.2/1.3;
OS Ranoidea gilleni (Centralian tree frog) (Litoria gilleni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Pelodryadinae; Ranoidea.
OX NCBI_TaxID=39405;
RN [1]
RP PROTEIN SEQUENCE, AMIDATION AT LEU-12, AND MASS SPECTROMETRY.
RC TISSUE=Parotoid gland;
RA Waugh R.J., Stone D.J.M., Bowie J.H., Wallace J.C., Tyler M.J.;
RT "Peptides from Australian frogs. The structures of the caerins and
RT caeridins from Litoria gilleni.";
RL J. Chem. Res. 139:937-961(1993).
RN [2]
RP PROTEIN SEQUENCE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Waugh R.J., Steinborner S.T., Bowie J.H., Wallace J.C., Tyler M.J., Hu P.,
RA Gross M.L.;
RT "Two isomeric alpha and beta aspartyl dodecapeptides and their cyclic amino
RT succinyl analogue from the Australian tree frog Litoria gilleni.";
RL Aust. J. Chem. 48:1981-1987(1995).
CC -!- FUNCTION: Caeridins show neither neuropeptide activity nor antibiotic
CC activity.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the skin parotoid and/or rostral
CC glands.
CC -!- PTM: Isomerization alpha-beta of the Asp-4 residue in caeridin 1.2; a
CC cyclic succinimide may be formed between Asp-4 and Gly-5 residues in
CC caeridin 1.3.
CC -!- MASS SPECTROMETRY: Mass=1140; Method=FAB; Evidence={ECO:0000269|Ref.1};
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DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Amidation; Amphibian defense peptide; Direct protein sequencing; Secreted.
FT PEPTIDE 1..12
FT /note="Caeridin-1.1/1.2/1.3"
FT /id="PRO_0000043756"
FT MOD_RES 12
FT /note="Leucine amide"
FT /evidence="ECO:0000269|Ref.1"
SQ SEQUENCE 12 AA; 1141 MW; 2822551A33772728 CRC64;
GLLDGLLGTL GL